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Volumn 5, Issue 4, 2015, Pages 2808-2839

HIV-1 recruits UPF1 but excludes UPF2 to promote nucleocytoplasmic export of the genomic RNA

Author keywords

HIV 1; Nonsense mediated decay; Nuclear RNA export; Ribonucleoprotein; UPF1; Viral evasion

Indexed keywords

EXPORTIN 1; GAG PROTEIN; GENOMIC RNA; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; ISOPROTEIN; PEPTIDES AND PROTEINS; PROTEIN P62; REV PROTEIN; UNCLASSIFIED DRUG; UPFRAMESHIFT PROTEIN 1; CELL RECEPTOR; DDX3X PROTEIN, HUMAN; DEAD BOX PROTEIN; EXPORTIN 1 PROTEIN; KARYOPHERIN; MEMBRANE PROTEIN; NUCLEAR PORE PROTEIN P62; NUCLEOPORIN; PROTEIN BINDING; RNA BINDING PROTEIN; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; UPF1 PROTEIN, HUMAN; UPF2 PROTEIN, HUMAN; UPF3A PROTEIN, HUMAN; VIRUS RNA;

EID: 85012088619     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5042808     Document Type: Article
Times cited : (47)

References (97)
  • 1
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • Cullen, B.R. Nuclear mRNA export: Insights from virology. Trends Biochem. Sci. 2003, 28, 419-424.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 2
    • 79960631283 scopus 로고    scopus 로고
    • Nuclear export dynamics of RNA-protein complexes
    • Grunwald, D.; Singer, R.H.; Rout, M. Nuclear export dynamics of RNA-protein complexes. Nature 2011, 475, 333-341.
    • (2011) Nature , vol.475 , pp. 333-341
    • Grunwald, D.1    Singer, R.H.2    Rout, M.3
  • 3
    • 0035827686 scopus 로고    scopus 로고
    • Overexpression of tap/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export
    • Braun, I.C.; Herold, A.; Rode, M.; Conti, E.; Izaurralde, E. Overexpression of tap/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export. J. Biol. Chem. 2001, 276, 20536-20543.
    • (2001) J. Biol. Chem , vol.276 , pp. 20536-20543
    • Braun, I.C.1    Herold, A.2    Rode, M.3    Conti, E.4    Izaurralde, E.5
  • 6
    • 84863760251 scopus 로고    scopus 로고
    • The human T-lymphotropic virus type 1 tax protein inhibits nonsense-mediated mRNA decay by interacting with INT6/EIF3E and UPF1
    • Mocquet, V.; Neusiedler, J.; Rende, F.; Cluet, D.; Robin, J.P.; Terme, J.M.; Duc Dodon, M.; Wittmann, J.; Morris, C.; le Hir, H.; et al. The human T-lymphotropic virus type 1 tax protein inhibits nonsense-mediated mRNA decay by interacting with INT6/EIF3E and UPF1. J. Virol. 2012, 86, 7530-7543.
    • (2012) J. Virol , vol.86 , pp. 7530-7543
    • Mocquet, V.1    Neusiedler, J.2    Rende, F.3    Cluet, D.4    Robin, J.P.5    Terme, J.M.6    Duc Dodon, M.7    Wittmann, J.8    Morris, C.9    le Hir, H.10
  • 7
    • 84879167304 scopus 로고    scopus 로고
    • Viral interference with host mRNA surveillance, the nonsense-mediated mRNA decay (NMD) pathway, through a new function of HTLV-1 Rex: Implications for retroviral replication
    • Nakano, K.; Ando, T.; Yamagishi, M.; Yokoyama, K.; Ishida, T.; Ohsugi, T.; Tanaka, Y.; Brighty, D.W.; Watanabe, T. Viral interference with host mRNA surveillance, the nonsense-mediated mRNA decay (NMD) pathway, through a new function of HTLV-1 Rex: Implications for retroviral replication. Microbes Infect. 2013, 15, 491-505.
    • (2013) Microbes Infect , vol.15 , pp. 491-505
    • Nakano, K.1    Ando, T.2    Yamagishi, M.3    Yokoyama, K.4    Ishida, T.5    Ohsugi, T.6    Tanaka, Y.7    Brighty, D.W.8    Watanabe, T.9
  • 8
    • 0027494083 scopus 로고
    • Alternative splicing of human immunodeficiency virus type 1 mRNA modulates viral protein expression, replication, and infectivity
    • Purcell, D.F.; Martin, M.A. Alternative splicing of human immunodeficiency virus type 1 mRNA modulates viral protein expression, replication, and infectivity. J. Virol. 1993, 67, 6365-6378.
    • (1993) J. Virol , vol.67 , pp. 6365-6378
    • Purcell, D.F.1    Martin, M.A.2
  • 9
    • 0024518918 scopus 로고
    • The HIV-1 Rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim, M.H.; Hauber, J.; Le, S.Y.; Maizel, J.V.; Cullen, B.R. The HIV-1 Rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 1989, 338, 254-257.
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 10
    • 0035809913 scopus 로고    scopus 로고
    • Cofactor requirements for nuclear export of Rev response element (RRE)-and constitutive transport element (CTE)-containing retroviral RNAs: An unexpected role for actin
    • Hofmann, W.; Reichart, B.; Ewald, A.; Muller, E.; Schmitt, I.; Stauber, R.H.; Lottspeich, F.; Jockusch, B.M.; Scheer, U.; Hauber, J.; et al. Cofactor requirements for nuclear export of Rev response element (RRE)-and constitutive transport element (CTE)-containing retroviral RNAs: An unexpected role for actin. J. Cell Biol 2001, 152, 895-910.
    • (2001) J. Cell Biol , vol.152 , pp. 895-910
    • Hofmann, W.1    Reichart, B.2    Ewald, A.3    Muller, E.4    Schmitt, I.5    Stauber, R.H.6    Lottspeich, F.7    Jockusch, B.M.8    Scheer, U.9    Hauber, J.10
  • 11
    • 0034565018 scopus 로고    scopus 로고
    • Rev protein and its cellular partners
    • Kjems, J.; Askjaer, P. Rev protein and its cellular partners. Adv. Pharmacol. 2000, 48, 251-298.
    • (2000) Adv. Pharmacol , vol.48 , pp. 251-298
    • Kjems, J.1    Askjaer, P.2
  • 12
    • 7044253474 scopus 로고    scopus 로고
    • Requirement of DDX3 dead box RNA helicase for HIV-1 Rev-RRE export function
    • Yedavalli, V.S.; Neuveut, C.; Chi, Y.H.; Kleiman, L.; Jeang, K.T. Requirement of DDX3 dead box RNA helicase for HIV-1 Rev-RRE export function. Cell 2004, 119, 381-392.
    • (2004) Cell , vol.119 , pp. 381-392
    • Yedavalli, V.S.1    Neuveut, C.2    Chi, Y.H.3    Kleiman, L.4    Jeang, K.T.5
  • 13
    • 13944267564 scopus 로고    scopus 로고
    • Sam68 is absolutely required for Rev function and HIV-1 production
    • Modem, S.; Badri, K.R.; Holland, T.C.; Reddy, T.R. Sam68 is absolutely required for Rev function and HIV-1 production. Nucleic Acids Res. 2005, 33, 873-879.
    • (2005) Nucleic Acids Res , vol.33 , pp. 873-879
    • Modem, S.1    Badri, K.R.2    Holland, T.C.3    Reddy, T.R.4
  • 14
    • 0034721040 scopus 로고    scopus 로고
    • Sam68, RNA helicase a and tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA
    • Reddy, T.R.; Tang, H.; Xu, W.; Wong-Staal, F. Sam68, RNA helicase a and tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA. Oncogene 2000, 19, 3570-3575.
    • (2000) Oncogene , vol.19 , pp. 3570-3575
    • Reddy, T.R.1    Tang, H.2    Xu, W.3    Wong-Staal, F.4
  • 15
    • 79958238205 scopus 로고    scopus 로고
    • HIV-1 remodels the nuclear pore complex
    • Monette, A.; Pante, N.; Mouland, A.J. HIV-1 remodels the nuclear pore complex. J. Cell Biol. 2011, 193, 619-631.
    • (2011) J. Cell Biol , vol.193 , pp. 619-631
    • Monette, A.1    Pante, N.2    Mouland, A.J.3
  • 16
    • 36849085461 scopus 로고    scopus 로고
    • An anti-apoptotic protein, HAX-1, inhibits the HIV-1 Rev function by altering its sub-cellular localization
    • Modem, S.; Reddy, T.R. An anti-apoptotic protein, HAX-1, inhibits the HIV-1 Rev function by altering its sub-cellular localization. J. Cell Physiol. 2008, 214, 14-19.
    • (2008) J. Cell Physiol , vol.214 , pp. 14-19
    • Modem, S.1    Reddy, T.R.2
  • 17
    • 70349840709 scopus 로고    scopus 로고
    • Insulin-like growth factor II mRNA binding protein 1 modulates Rev-dependent human immunodeficiency virus type 1 RNA expression
    • Zhou, Y.; Rong, L.; Zhang, J.; Aloysius, C.; Pan, Q.; Liang, C. Insulin-like growth factor II mRNA binding protein 1 modulates Rev-dependent human immunodeficiency virus type 1 RNA expression. Virology 2009, 393, 210-220.
    • (2009) Virology , vol.393 , pp. 210-220
    • Zhou, Y.1    Rong, L.2    Zhang, J.3    Aloysius, C.4    Pan, Q.5    Liang, C.6
  • 18
    • 84857367885 scopus 로고    scopus 로고
    • Discovery of the first small molecule inhibitor of human DDX3 specifically designed to target the RNA binding site: Towards the next generation HIV-1 inhibitors
    • Radi, M.; Falchi, F.; Garbelli, A.; Samuele, A.; Bernardo, V.; Paolucci, S.; Baldanti, F.; Schenone, S.; Manetti, F.; Maga, G.; et al. Discovery of the first small molecule inhibitor of human DDX3 specifically designed to target the RNA binding site: Towards the next generation HIV-1 inhibitors. Bioorg. Med. Chem. Lett. 2012, 22, 2094-2098.
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 2094-2098
    • Radi, M.1    Falchi, F.2    Garbelli, A.3    Samuele, A.4    Bernardo, V.5    Paolucci, S.6    Baldanti, F.7    Schenone, S.8    Manetti, F.9    Maga, G.10
  • 19
    • 77949904260 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in human cells: Mechanistic insights, functions beyond quality control and the double-life of nmd factors
    • Nicholson, P.; Yepiskoposyan, H.; Metze, S.; Orozco, R.Z.; Kleinschmidt, N.; Muhlemann, O. Nonsense-mediated mRNA decay in human cells: Mechanistic insights, functions beyond quality control and the double-life of nmd factors. Cell Mol. Life Sci. 2010, 67, 677-700.
    • (2010) Cell Mol. Life Sci , vol.67 , pp. 677-700
    • Nicholson, P.1    Yepiskoposyan, H.2    Metze, S.3    Orozco, R.Z.4    Kleinschmidt, N.5    Muhlemann, O.6
  • 20
    • 59649124310 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay (NMD) mechanisms
    • Brogna, S.; Wen, J. Nonsense-mediated mRNA decay (NMD) mechanisms. Nat. Struct. Mol. Biol. 2009, 16, 107-113.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 107-113
    • Brogna, S.1    Wen, J.2
  • 21
    • 0037064145 scopus 로고    scopus 로고
    • Separable roles for RENT1/HUPF1 in altered splicing and decay of nonsense transcripts
    • Mendell, J.T.; ap Rhys, C.M.; Dietz, H.C. Separable roles for RENT1/HUPF1 in altered splicing and decay of nonsense transcripts. Science 2002, 298, 419-422.
    • (2002) Science , vol.298 , pp. 419-422
    • Mendell, J.T.1    ap Rhys, C.M.2    Dietz, H.C.3
  • 22
    • 49949105213 scopus 로고    scopus 로고
    • The multiple lives of nmd factors: Balancing roles in gene and genome regulation
    • Isken, O.; Maquat, L.E. The multiple lives of nmd factors: Balancing roles in gene and genome regulation. Nat. Rev. Genet. 2008, 9, 699-712.
    • (2008) Nat. Rev. Genet , vol.9 , pp. 699-712
    • Isken, O.1    Maquat, L.E.2
  • 23
    • 33745712580 scopus 로고    scopus 로고
    • Nuclear mRNA degradation pathway(s) are implicated in xist regulation and X chromosome inactivation
    • Ciaudo, C.; Bourdet, A.; Cohen-Tannoudji, M.; Dietz, H.C.; Rougeulle, C.; Avner, P. Nuclear mRNA degradation pathway(s) are implicated in xist regulation and X chromosome inactivation. PLoS Genet. 2006, 2, e94.
    • (2006) PLoS Genet , vol.2
    • Ciaudo, C.1    Bourdet, A.2    Cohen-Tannoudji, M.3    Dietz, H.C.4    Rougeulle, C.5    Avner, P.6
  • 24
    • 12944327374 scopus 로고    scopus 로고
    • Mammalian staufen1 recruits UPF1 to specific mRNA 3'-UTRs so as to elicit mRNA decay
    • Kim, Y.K.; Furic, L.; Desgroseillers, L.; Maquat, L.E. Mammalian staufen1 recruits UPF1 to specific mRNA 3'-UTRs so as to elicit mRNA decay. Cell 2005, 120, 195-208.
    • (2005) Cell , vol.120 , pp. 195-208
    • Kim, Y.K.1    Furic, L.2    Desgroseillers, L.3    Maquat, L.E.4
  • 25
    • 32944458421 scopus 로고    scopus 로고
    • The human RNA surveillance factor UPF1 is required for s phase progression and genome stability
    • Azzalin, C.M.; Lingner, J. The human RNA surveillance factor UPF1 is required for s phase progression and genome stability. Curr. Biol. 2006, 16, 433-439.
    • (2006) Curr. Biol , vol.16 , pp. 433-439
    • Azzalin, C.M.1    Lingner, J.2
  • 26
    • 80053615725 scopus 로고    scopus 로고
    • Human UPF1 interacts with TPP1 and telomerase and sustains telomere leading-strand replication
    • Chawla, R.; Redon, S.; Raftopoulou, C.; Wischnewski, H.; Gagos, S.; Azzalin, C.M. Human UPF1 interacts with TPP1 and telomerase and sustains telomere leading-strand replication. EMBO J. 2011, 30, 4047-4058.
    • (2011) EMBO J , vol.30 , pp. 4047-4058
    • Chawla, R.1    Redon, S.2    Raftopoulou, C.3    Wischnewski, H.4    Gagos, S.5    Azzalin, C.M.6
  • 27
    • 42449161413 scopus 로고    scopus 로고
    • The editing enzyme ADAR1 and the mRNA surveillance protein HUPF1 interact in the cell nucleus
    • Agranat, L.; Raitskin, O.; Sperling, J.; Sperling, R. The editing enzyme ADAR1 and the mRNA surveillance protein HUPF1 interact in the cell nucleus. Proc. Natl. Acad. Sci. USA 2008, 105, 5028-5033.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5028-5033
    • Agranat, L.1    Raitskin, O.2    Sperling, J.3    Sperling, R.4
  • 28
    • 37849005006 scopus 로고    scopus 로고
    • NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity
    • Chamieh, H.; Ballut, L.; Bonneau, F.; le Hir, H. NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity. Nat. Struct. Mol. Biol. 2008, 15, 85-93.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 85-93
    • Chamieh, H.1    Ballut, L.2    Bonneau, F.3    le Hir, H.4
  • 29
    • 40949148553 scopus 로고    scopus 로고
    • Interactions between UPF1, ERFS, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
    • Ivanov, P.V.; Gehring, N.H.; Kunz, J.B.; Hentze, M.W.; Kulozik, A.E. Interactions between UPF1, ERFS, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways. EMBO J. 2008, 27, 736-747.
    • (2008) EMBO J , vol.27 , pp. 736-747
    • Ivanov, P.V.1    Gehring, N.H.2    Kunz, J.B.3    Hentze, M.W.4    Kulozik, A.E.5
  • 30
    • 32044435368 scopus 로고    scopus 로고
    • Binding of a novel smg-1-UPF1-ERF1-ERF3 complex (SURF) to the exon junction complex triggers UPF1 phosphorylation and nonsense-mediated mRNA decay
    • Kashima, I.; Yamashita, A.; Izumi, N.; Kataoka, N.; Morishita, R.; Hoshino, S.; Ohno, M.; Dreyfuss, G.; Ohno, S. Binding of a novel smg-1-UPF1-ERF1-ERF3 complex (SURF) to the exon junction complex triggers UPF1 phosphorylation and nonsense-mediated mRNA decay. Genes Dev. 2006, 20, 355-367.
    • (2006) Genes Dev , vol.20 , pp. 355-367
    • Kashima, I.1    Yamashita, A.2    Izumi, N.3    Kataoka, N.4    Morishita, R.5    Hoshino, S.6    Ohno, M.7    Dreyfuss, G.8    Ohno, S.9
  • 32
    • 0033835231 scopus 로고    scopus 로고
    • Characterization of the biochemical properties of the human UPF1 gene product that is involved in nonsense-mediated mRNA decay
    • Bhattacharya, A.; Czaplinski, K.; Trifillis, P.; He, F.; Jacobson, A.; Peltz, S.W. Characterization of the biochemical properties of the human UPF1 gene product that is involved in nonsense-mediated mRNA decay. RNA 2000, 6, 1226-1235.
    • (2000) RNA , vol.6 , pp. 1226-1235
    • Bhattacharya, A.1    Czaplinski, K.2    Trifillis, P.3    He, F.4    Jacobson, A.5    Peltz, S.W.6
  • 33
    • 66049162655 scopus 로고    scopus 로고
    • Execution of nonsense-mediated mRNA decay: What defines a substrate?
    • Rebbapragada, I.; Lykke-Andersen, J. Execution of nonsense-mediated mRNA decay: What defines a substrate? Curr. Opin. Cell Biol. 2009, 21, 394-402.
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 394-402
    • Rebbapragada, I.1    Lykke-Andersen, J.2
  • 35
    • 81755172088 scopus 로고    scopus 로고
    • Autoregulation of the nonsense-mediated mRNA decay pathway in human cells
    • Yepiskoposyan, H.; Aeschimann, F.; Nilsson, D.; Okoniewski, M.; Muhlemann, O. Autoregulation of the nonsense-mediated mRNA decay pathway in human cells. RNA 2011, 17, 2108-2118.
    • (2011) RNA , vol.17 , pp. 2108-2118
    • Yepiskoposyan, H.1    Aeschimann, F.2    Nilsson, D.3    Okoniewski, M.4    Muhlemann, O.5
  • 39
    • 84881477715 scopus 로고    scopus 로고
    • Translation-dependent displacement of UPF1 from coding sequences causes its enrichment in 3'-UTRs
    • Zund, D.; Gruber, A.R.; Zavolan, M.; Muhlemann, O. Translation-dependent displacement of UPF1 from coding sequences causes its enrichment in 3'-UTRs. Nat. Struct. Mol. Biol. 2013, 20, 936-943.
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 936-943
    • Zund, D.1    Gruber, A.R.2    Zavolan, M.3    Muhlemann, O.4
  • 40
    • 84885069820 scopus 로고    scopus 로고
    • Global analyses of UPF1 binding and function reveal expanded scope of nonsense-mediated mRNA decay
    • Hurt, J.A.; Robertson, A.D.; Burge, C.B. Global analyses of UPF1 binding and function reveal expanded scope of nonsense-mediated mRNA decay. Genome Res. 2013, 23, 1636-1650.
    • (2013) Genome Res , vol.23 , pp. 1636-1650
    • Hurt, J.A.1    Robertson, A.D.2    Burge, C.B.3
  • 41
    • 25844512736 scopus 로고    scopus 로고
    • Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements
    • Gehring, N.H.; Kunz, J.B.; Neu-Yilik, G.; Breit, S.; Viegas, M.H.; Hentze, M.W.; Kulozik, A.E. Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements. Mol. Cell 2005, 20, 65-75.
    • (2005) Mol. Cell , vol.20 , pp. 65-75
    • Gehring, N.H.1    Kunz, J.B.2    Neu-Yilik, G.3    Breit, S.4    Viegas, M.H.5    Hentze, M.W.6    Kulozik, A.E.7
  • 42
    • 66249097064 scopus 로고    scopus 로고
    • Long 3'-UTRs target wild-type mRNAs for nonsense-mediated mRNA decay in saccharomyces cerevisiae
    • Kebaara, B.W.; Atkin, A.L. Long 3'-UTRs target wild-type mRNAs for nonsense-mediated mRNA decay in saccharomyces cerevisiae. Nucleic Acids Res. 2009, 37, 2771-2778.
    • (2009) Nucleic Acids Res , vol.37 , pp. 2771-2778
    • Kebaara, B.W.1    Atkin, A.L.2
  • 43
    • 80055011827 scopus 로고    scopus 로고
    • The structure and function of the rous sarcoma virus RNA stability element
    • Withers, J.B.; Beemon, K.L. The structure and function of the rous sarcoma virus RNA stability element. J. Cell. Biochem. 2011, 112, 3085-3092.
    • (2011) J. Cell. Biochem , vol.112 , pp. 3085-3092
    • Withers, J.B.1    Beemon, K.L.2
  • 44
    • 79960558747 scopus 로고    scopus 로고
    • Characterization of the HIV-1 RNA associated proteome identifies matrin 3 as a nuclear cofactor of Rev function
    • Kula, A.; Guerra, J.; Knezevich, A.; Kleva, D.; Myers, M.P.; Marcello, A. Characterization of the HIV-1 RNA associated proteome identifies matrin 3 as a nuclear cofactor of Rev function. Retrovirology 2011, doi:10.1186/1742-4690-8-60.
    • (2011) Retrovirology
    • Kula, A.1    Guerra, J.2    Knezevich, A.3    Kleva, D.4    Myers, M.P.5    Marcello, A.6
  • 45
    • 84875793133 scopus 로고    scopus 로고
    • Characterization of staufen1 ribonucleoproteins by mass spectrometry and biochemical analyses reveal the presence of diverse host proteins associated with human immunodeficiency virus type 1
    • Milev, M.P.; Ravichandran, M.; Khan, M.F.; Schriemer, D.C.; Mouland, A.J. Characterization of staufen1 ribonucleoproteins by mass spectrometry and biochemical analyses reveal the presence of diverse host proteins associated with human immunodeficiency virus type 1. Front. Microbiol. 2012, doi:10.3389/fmicb.2012.00367.
    • (2012) Front. Microbiol
    • Milev, M.P.1    Ravichandran, M.2    Khan, M.F.3    Schriemer, D.C.4    Mouland, A.J.5
  • 46
    • 77958459763 scopus 로고    scopus 로고
    • UPF1 senses 3'-UTR length to potentiate mRNA decay
    • Hogg, J.R.; Goff, S.P. UPF1 senses 3'-UTR length to potentiate mRNA decay. Cell 2010, 143, 379-389.
    • (2010) Cell , vol.143 , pp. 379-389
    • Hogg, J.R.1    Goff, S.P.2
  • 47
    • 33646865949 scopus 로고    scopus 로고
    • Functions of HUPF3A and HUPF3B in nonsense-mediated mRNA decay and translation
    • Kunz, J.B.; Neu-Yilik, G.; Hentze, M.W.; Kulozik, A.E.; Gehring, N.H. Functions of HUPF3A and HUPF3B in nonsense-mediated mRNA decay and translation. RNA 2006, 12, 1015-1022.
    • (2006) RNA , vol.12 , pp. 1015-1022
    • Kunz, J.B.1    Neu-Yilik, G.2    Hentze, M.W.3    Kulozik, A.E.4    Gehring, N.H.5
  • 48
    • 0034751160 scopus 로고    scopus 로고
    • Identification and characterization of human orthologues to saccharomyces cerevisiae UPF2 protein and UPF3 protein (caenorhabditis elegans SMG-4)
    • Serin, G.; Gersappe, A.; Black, J.D.; Aronoff, R.; Maquat, L.E. Identification and characterization of human orthologues to saccharomyces cerevisiae UPF2 protein and UPF3 protein (caenorhabditis elegans SMG-4). Mol. Cell Biol. 2001, 21, 209-223.
    • (2001) Mol. Cell Biol , vol.21 , pp. 209-223
    • Serin, G.1    Gersappe, A.2    Black, J.D.3    Aronoff, R.4    Maquat, L.E.5
  • 50
    • 84856858152 scopus 로고    scopus 로고
    • N- and C-terminal UPF1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD
    • Okada-Katsuhata, Y.; Yamashita, A.; Kutsuzawa, K.; Izumi, N.; Hirahara, F.; Ohno, S. N- and C-terminal UPF1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD. Nucleic Acids Res. 2012, 40, 1251-1266.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1251-1266
    • Okada-Katsuhata, Y.1    Yamashita, A.2    Kutsuzawa, K.3    Izumi, N.4    Hirahara, F.5    Ohno, S.6
  • 51
    • 0033527576 scopus 로고    scopus 로고
    • The human tap nuclear RNA export factor contains a novel transportin-dependent nuclear localization signal that lacks nuclear export signal function
    • Truant, R.; Kang, Y.; Cullen, B.R. The human tap nuclear RNA export factor contains a novel transportin-dependent nuclear localization signal that lacks nuclear export signal function. J. Biol. Chem. 1999, 274, 32167-32171.
    • (1999) J. Biol. Chem , vol.274 , pp. 32167-32171
    • Truant, R.1    Kang, Y.2    Cullen, B.R.3
  • 52
    • 34047201192 scopus 로고    scopus 로고
    • Live-cell assay for simultaneous monitoring of expression and interaction of proteins
    • Wolff, H.; Hartl, A.; Eilken, H.M.; Hadian, K.; Ziegler, M.; Brack-Werner, R. Live-cell assay for simultaneous monitoring of expression and interaction of proteins. Biotechniques 2006, 41, 690-692.
    • (2006) Biotechniques , vol.41 , pp. 690-692
    • Wolff, H.1    Hartl, A.2    Eilken, H.M.3    Hadian, K.4    Ziegler, M.5    Brack-Werner, R.6
  • 54
    • 69949118279 scopus 로고    scopus 로고
    • Inhibition of nonsense-mediated mRNA decay by the natural product pateamine a through eukaryotic initiation factor 4AIII
    • Dang, Y.; Low, W.K.; Xu, J.; Gehring, N.H.; Dietz, H.C.; Romo, D.; Liu, J.O. Inhibition of nonsense-mediated mRNA decay by the natural product pateamine a through eukaryotic initiation factor 4AIII. J. Biol. Chem. 2009, 284, 23613-23621.
    • (2009) J. Biol. Chem , vol.284 , pp. 23613-23621
    • Dang, Y.1    Low, W.K.2    Xu, J.3    Gehring, N.H.4    Dietz, H.C.5    Romo, D.6    Liu, J.O.7
  • 55
    • 0034460323 scopus 로고    scopus 로고
    • Novel UPF2P orthologues suggest a functional link between translation initiation and nonsense surveillance complexes
    • Mendell, J.T.; Medghalchi, S.M.; Lake, R.G.; Noensie, E.N.; Dietz, H.C. Novel UPF2P orthologues suggest a functional link between translation initiation and nonsense surveillance complexes. Mol. Cell Biol. 2000, 20, 8944-8957.
    • (2000) Mol. Cell Biol , vol.20 , pp. 8944-8957
    • Mendell, J.T.1    Medghalchi, S.M.2    Lake, R.G.3    Noensie, E.N.4    Dietz, H.C.5
  • 56
    • 71449106849 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: Implications for HIV-1 gene expression
    • Monette, A.; Ajamian, L.; Lopez-Lastra, M.; Mouland, A.J. Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: Implications for HIV-1 gene expression. J. Biol. Chem. 2009, 284, 31350-31362.
    • (2009) J. Biol. Chem , vol.284 , pp. 31350-31362
    • Monette, A.1    Ajamian, L.2    Lopez-Lastra, M.3    Mouland, A.J.4
  • 57
    • 34249937436 scopus 로고    scopus 로고
    • The host protein staufen1 participates in human immunodeficiency virus type 1 assembly in live cells by influencing pr55Gag multimerization
    • Chatel-Chaix, L.; Abrahamyan, L.; Frechina, C.; Mouland, A.J.; des Groseillers, L. The host protein staufen1 participates in human immunodeficiency virus type 1 assembly in live cells by influencing pr55Gag multimerization. J. Virol. 2007, 81, 6216-6230.
    • (2007) J. Virol , vol.81 , pp. 6216-6230
    • Chatel-Chaix, L.1    Abrahamyan, L.2    Frechina, C.3    Mouland, A.J.4    des Groseillers, L.5
  • 58
    • 67649598052 scopus 로고    scopus 로고
    • Intracellular transport of human immunodeficiency virus type 1 genomic RNA and viral production are dependent on dynein motor function and late endosome positioning
    • Lehmann, M.; Milev, M.P.; Abrahamyan, L.; Yao, X.J.; Pante, N.; Mouland, A.J. Intracellular transport of human immunodeficiency virus type 1 genomic RNA and viral production are dependent on dynein motor function and late endosome positioning. J. Biol. Chem. 2009, 284, 14572-14585.
    • (2009) J. Biol. Chem , vol.284 , pp. 14572-14585
    • Lehmann, M.1    Milev, M.P.2    Abrahamyan, L.3    Yao, X.J.4    Pante, N.5    Mouland, A.J.6
  • 60
    • 84863763633 scopus 로고    scopus 로고
    • Detection of viral RNA by fluorescence in situ hybridization (fish)
    • Vyboh, K.; Ajamian, L.; Mouland, A.J. Detection of viral RNA by fluorescence in situ hybridization (fish). J. Vis. Exp. 2012, doi:10.3791/4002.
    • (2012) J. Vis. Exp
    • Vyboh, K.1    Ajamian, L.2    Mouland, A.J.3
  • 63
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • Jouvenet, N.; Bieniasz, P.D.; Simon, S.M. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 2008, 454, 236-240.
    • (2008) Nature , vol.454 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 64
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B.; Wehrly, K.; Nishio, J.; Perryman, S. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism. J. Virol. 1992, 66, 6547-6554.
    • (1992) J. Virol , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 65
    • 0141457246 scopus 로고    scopus 로고
    • Control of HIV-1 ENV RNA splicing and transport: Investigating the role of hnRNP A1 in exon splicing silencer (ESS3A) function
    • Asai, K.; Platt, C.; Cochrane, A. Control of HIV-1 ENV RNA splicing and transport: Investigating the role of hnRNP A1 in exon splicing silencer (ESS3A) function. Virology 2003, 314, 229-242.
    • (2003) Virology , vol.314 , pp. 229-242
    • Asai, K.1    Platt, C.2    Cochrane, A.3
  • 66
    • 0034035072 scopus 로고    scopus 로고
    • The double-stranded RNA-binding protein staufen is incorporated in human immunodeficiency virus type 1: Evidence for a role in genomic RNA encapsidation
    • Mouland, A.J.; Mercier, J.; Luo, M.; Bernier, L.; DesGroseillers, L.; Cohen, E.A. The double-stranded RNA-binding protein staufen is incorporated in human immunodeficiency virus type 1: Evidence for a role in genomic RNA encapsidation. J. Virol. 2000, 74, 5441-5451.
    • (2000) J. Virol , vol.74 , pp. 5441-5451
    • Mouland, A.J.1    Mercier, J.2    Luo, M.3    Bernier, L.4    DesGroseillers, L.5    Cohen, E.A.6
  • 69
    • 77955446835 scopus 로고    scopus 로고
    • HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes
    • Daugherty, M.D.; Booth, D.S.; Jayaraman, B.; Cheng, Y.; Frankel, A.D. HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes. Proc. Natl. Acad. Sci. USA 2010, 107, 12481-12486.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12481-12486
    • Daugherty, M.D.1    Booth, D.S.2    Jayaraman, B.3    Cheng, Y.4    Frankel, A.D.5
  • 73
    • 85012085620 scopus 로고    scopus 로고
    • McGill University, Montreal, Canada. Unpublished data
    • Ajamian, L.; Mouland, A.J. McGill University, Montreal, Canada. Unpublished data, 2015.
    • (2015)
    • Ajamian, L.1    Mouland, A.J.2
  • 74
    • 58149520665 scopus 로고    scopus 로고
    • SMD and NMD are competitive pathways that contribute to myogenesis: Effects on PAX3 and myogenin mRNAs
    • Gong, C.; Kim, Y.K.; Woeller, C.F.; Tang, Y.; Maquat, L.E. SMD and NMD are competitive pathways that contribute to myogenesis: Effects on PAX3 and myogenin mRNAs. Genes Dev. 2009, 23, 54-66.
    • (2009) Genes Dev , vol.23 , pp. 54-66
    • Gong, C.1    Kim, Y.K.2    Woeller, C.F.3    Tang, Y.4    Maquat, L.E.5
  • 75
    • 13644266893 scopus 로고    scopus 로고
    • UPF1p, a highly conserved protein required for nonsense-mediated mRNA decay, interacts with the nuclear pore proteins NUP100P and NUP116P
    • Nazarenus, T.; Cedarberg, R.; Bell, R.; Cheatle, J.; Forch, A.; Haifley, A.; Hou, A.; Kebaara, B.W.; Shields, C.; Stoysich, K.; et al. UPF1p, a highly conserved protein required for nonsense-mediated mRNA decay, interacts with the nuclear pore proteins NUP100P and NUP116P. Gene 2005, 345, 199-212.
    • (2005) Gene , vol.345 , pp. 199-212
    • Nazarenus, T.1    Cedarberg, R.2    Bell, R.3    Cheatle, J.4    Forch, A.5    Haifley, A.6    Hou, A.7    Kebaara, B.W.8    Shields, C.9    Stoysich, K.10
  • 76
    • 84864799957 scopus 로고    scopus 로고
    • Virus-producing cells determine the host protein profiles of HIV-1 virion cores
    • Santos, S.; Obukhov, Y.; Nekhai, S.; Bukrinsky, M.; Iordanskiy, S. Virus-producing cells determine the host protein profiles of HIV-1 virion cores. Retrovirology 2012, doi:10.1186/1742-4690-9-65.
    • (2012) Retrovirology
    • Santos, S.1    Obukhov, Y.2    Nekhai, S.3    Bukrinsky, M.4    Iordanskiy, S.5
  • 77
    • 0030745114 scopus 로고    scopus 로고
    • Cloning and characterization of HUPF1, a human homolog of the saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein
    • Applequist, S.E.; Selg, M.; Raman, C.; Jack, H.M. Cloning and characterization of HUPF1, a human homolog of the saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein. Nucleic Acids Res. 1997, 25, 814-821.
    • (1997) Nucleic Acids Res , vol.25 , pp. 814-821
    • Applequist, S.E.1    Selg, M.2    Raman, C.3    Jack, H.M.4
  • 78
    • 18144403878 scopus 로고    scopus 로고
    • Within you, without you: HIV-1 Rev and RNA export
    • Dayton, A.I. Within you, without you: HIV-1 Rev and RNA export. Retrovirology 2004, doi:10.1186/ 1742-4690-1-35.
    • (2004) Retrovirology
    • Dayton, A.I.1
  • 79
    • 59649120307 scopus 로고    scopus 로고
    • Cellular proteins and HIV-1 Rev function
    • Suhasini, M.; Reddy, T.R. Cellular proteins and HIV-1 Rev function. Curr. HIV Res. 2009, 7, 91-100.
    • (2009) Curr. HIV Res , vol.7 , pp. 91-100
    • Suhasini, M.1    Reddy, T.R.2
  • 80
    • 77951969691 scopus 로고    scopus 로고
    • Live cell visualization of the interactions between HIV-1 Gag and the cellular RNA-binding protein Staufen1
    • Milev, M.P.; Brown, C.M.; Mouland, A.J. Live cell visualization of the interactions between HIV-1 Gag and the cellular RNA-binding protein Staufen1. Retrovirology 2010, doi:10.1186/1742-4690-7-41.
    • (2010) Retrovirology
    • Milev, M.P.1    Brown, C.M.2    Mouland, A.J.3
  • 81
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M.; Ohno, M.; Yoshida, M.; Mattaj, I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997, 90, 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 82
    • 84897980054 scopus 로고    scopus 로고
    • Zdock server: Interactive docking prediction of protein-protein complexes and symmetric multimers
    • Pierce, B.G.; Wiehe, K.; Hwang, H.; Kim, B.H.; Vreven, T.; Weng, Z. Zdock server: Interactive docking prediction of protein-protein complexes and symmetric multimers. Bioinformatics 2014, 30, 1771-1773.
    • (2014) Bioinformatics , vol.30 , pp. 1771-1773
    • Pierce, B.G.1    Wiehe, K.2    Hwang, H.3    Kim, B.H.4    Vreven, T.5    Weng, Z.6
  • 83
    • 33749239197 scopus 로고    scopus 로고
    • Crystal structure of the UPF2-interacting domain of nonsense-mediated mRNA decay factor UPF1
    • Kadlec, J.; Guilligay, D.; Ravelli, R.B.; Cusack, S. Crystal structure of the UPF2-interacting domain of nonsense-mediated mRNA decay factor UPF1. RNA 2006, 12, 1817-1824.
    • (2006) RNA , vol.12 , pp. 1817-1824
    • Kadlec, J.1    Guilligay, D.2    Ravelli, R.B.3    Cusack, S.4
  • 84
    • 81755161588 scopus 로고    scopus 로고
    • Cotranscriptional effect of a premature termination codon revealed by live-cell imaging
    • De Turris, V.; Nicholson, P.; Orozco, R.Z.; Singer, R.H.; Muhlemann, O. Cotranscriptional effect of a premature termination codon revealed by live-cell imaging. RNA 2011, 17, 2094-2107.
    • (2011) RNA , vol.17 , pp. 2094-2107
    • De Turris, V.1    Nicholson, P.2    Orozco, R.Z.3    Singer, R.H.4    Muhlemann, O.5
  • 86
    • 84881222279 scopus 로고    scopus 로고
    • UPF1 is crucial for the infectivity of human immunodeficiency virus type 1 progeny virions
    • Serquina, A.K.; Das, S.R.; Popova, E.; Ojelabi, O.A.; Roy, C.K.; Gottlinger, H.G. UPF1 is crucial for the infectivity of human immunodeficiency virus type 1 progeny virions. J. Virol. 2013, 87, 8853-8861.
    • (2013) J. Virol , vol.87 , pp. 8853-8861
    • Serquina, A.K.1    Das, S.R.2    Popova, E.3    Ojelabi, O.A.4    Roy, C.K.5    Gottlinger, H.G.6
  • 87
    • 85003260887 scopus 로고    scopus 로고
    • The export receptor CRM1 forms a dimer to promote nuclear export of HIV RNA
    • Booth, D.S.; Cheng, Y.; Frankel, A.D. The export receptor CRM1 forms a dimer to promote nuclear export of HIV RNA. eLife 2014, doi:10.7554/eLife.04121.
    • (2014) eLife
    • Booth, D.S.1    Cheng, Y.2    Frankel, A.D.3
  • 88
  • 89
    • 0032888954 scopus 로고    scopus 로고
    • Nucleoporins NUP98 and NUP214 participate in nuclear export of human immunodeficiency virus type 1 Rev
    • Zolotukhin, A.S.; Felber, B.K. Nucleoporins NUP98 and NUP214 participate in nuclear export of human immunodeficiency virus type 1 Rev. J. Virol. 1999, 73, 120-127.
    • (1999) J. Virol , vol.73 , pp. 120-127
    • Zolotukhin, A.S.1    Felber, B.K.2
  • 90
    • 33144460384 scopus 로고    scopus 로고
    • Ataxia-telangiectasia-mutated (ATM) protein can enhance human immunodeficiency virus type 1 replication by stimulating Rev function
    • Ariumi, Y.; Trono, D. Ataxia-telangiectasia-mutated (ATM) protein can enhance human immunodeficiency virus type 1 replication by stimulating Rev function. J. Virol. 2006, 80, 2445-2452.
    • (2006) J. Virol , vol.80 , pp. 2445-2452
    • Ariumi, Y.1    Trono, D.2
  • 92
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh, Y. ATM and related protein kinases: Safeguarding genome integrity. Nat. Rev. Cancer 2003, 3, 155-168.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 93
    • 69949191661 scopus 로고    scopus 로고
    • Aberrant mRNA transcripts and the nonsense-mediated decay proteins UPF2 and UPF3 are enriched in the arabidopsis nucleolus
    • Kim, S.H.; Koroleva, O.A.; Lewandowska, D.; Pendle, A.F.; Clark, G.P.; Simpson, C.G.; Shaw, P.J.; Brown, J.W. Aberrant mRNA transcripts and the nonsense-mediated decay proteins UPF2 and UPF3 are enriched in the arabidopsis nucleolus. Plant Cell 2009, 21, 2045-2057.
    • (2009) Plant Cell , vol.21 , pp. 2045-2057
    • Kim, S.H.1    Koroleva, O.A.2    Lewandowska, D.3    Pendle, A.F.4    Clark, G.P.5    Simpson, C.G.6    Shaw, P.J.7    Brown, J.W.8
  • 94
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of MRNP remodeling
    • Lejeune, F.; Ishigaki, Y.; Li, X.; Maquat, L.E. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of MRNP remodeling. EMBO J. 2002, 21, 3536-3545.
    • (2002) EMBO J , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 95
    • 70450182086 scopus 로고    scopus 로고
    • Gene expression networks: Competing mRNA decay pathways in mammalian cells
    • Maquat, L.E.; Gong, C. Gene expression networks: Competing mRNA decay pathways in mammalian cells. Biochem. Soc. Trans. 2009, 37, 1287-1292.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 1287-1292
    • Maquat, L.E.1    Gong, C.2
  • 96
    • 84864933811 scopus 로고    scopus 로고
    • Evidence that the UPF1-related molecular motor scans the 3'-UTR to ensure mRNA integrity
    • Shigeoka, T.; Kato, S.; Kawaichi, M.; Ishida, Y. Evidence that the UPF1-related molecular motor scans the 3'-UTR to ensure mRNA integrity. Nucleic Acids Res. 2012, 40, 6887-6897.
    • (2012) Nucleic Acids Res , vol.40 , pp. 6887-6897
    • Shigeoka, T.1    Kato, S.2    Kawaichi, M.3    Ishida, Y.4


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